The use of proteolysis and direct N-terminal sequence analysis to study human interleukin-2/receptor interaction on solid support.
An immobilized interleukin-2 receptor which is capable of binding interleukin-2 and suitable for direct N-terminal sequence analysis was employed to study interleukin-2/receptor interactions. Sensitive tryptic sites on the immobilized receptor and its interleukin-2 complex were identified by sequence analyses and compared. The results have revealed that the N-terminal region of interleukin-2 is not involved in receptor binding and the peptide segment covering residues 36-39 in the receptor is probably near or involved in the interleukin-2 binding site. The rapidity and simplicity make this solid phase sequence approach a good method for analyzing interleukin-2/receptor interaction and may be suitable for studying other protein-ligand interactions.
Pan
Y C
YC
Department of Protein Biochemistry, Hoffmann-La Roche Inc., Nutley, NJ.
Wang
F
F
Miedel
M C
MC
Weber
D V
DV
Bailon
P
P
Khan
F R
FR
Hulmes
J D
JD
D000595:Amino Acid Sequence; D002846:Chromatography, Affinity / Q000379:methods; D006801:Humans; D007376:Interleukin-2 / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D015375:Receptors, Interleukin-2 / Q000378:metabolism*; D014357:Trypsin
D007376:Interleukin-2; D010446:Peptide Fragments; D015375:Receptors, Interleukin-2; D014357:Trypsin